TABLE 1.
Crystal parameters, data collection, and structure refinement
| Apo form | Complex form | |
|---|---|---|
| Data collection | ||
| Space group | C2 | C2 |
| Unit cell | ||
| a, b, c (Å) | 183.28, 65.35, 126.69 | 184.03, 66.65, 133.35 |
| α, β, γ (degrees) | 90.00, 133.38, 90.00 | 90.00, 136.33, 90.00 |
| Resolution range (Å) | 42.9–2.0 | 46.0–2.4 |
| Unique reflections | 72,464 (10,190)a | 42,473 (5,887) |
| Completeness (%) | 98.8 (95.7) | 98.2 (94.6) |
| 〈I/σ(I)〉 | 8.8 (4.5) | 15.3 (6.5) |
| Rmergeb (%) | 8.3 (17.1) | 5.1 (11.2) |
| Average redundancy | 3.4 (3.2) | 3.5 (3.0) |
| Structure refinement | ||
| Resolution range (Å) | 31.7–2.0 | 46.0–2.4 |
| R factorc/R-freed (%) | 17.7/22.2 | 17.5/25.1 |
| No. of protein atoms | 7,504 | 7,522 |
| No. of water atoms | 579 | 202 |
| RMSDe bond lengths (Å) | 0.007 | 0.007 |
| RMSD bond angles (degrees) | 1.159 | 1.143 |
| Mean B factors (Å2) | 20.4 | 44.5 |
| Ramachandran plotf (residues, %) | ||
| Most favored (%) | 99.2 | 98.1 |
| Additional allowed (%) | 0.8 | 1.9 |
| Outliers (%) | 0 | 0 |
| Protein Data Bank entry | 4IPL | 4IPN |
a The values in parentheses refer to statistics in the highest bin.
b Rmerge = ΣhklΣi|Ii(hkl) − 〈I(hkl)〉|/ΣhklΣiIi(hkl), where Ii(hkl) is the intensity of an observation, and 〈I(hkl)〉 is the mean value for its unique reflection. Summations are over all reflections.
c R factor = Σh|Fo(h) − Fc(h)|/ΣhFo(h), where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
d R-free was calculated with 5% of the data excluded from the refinement.
e Root mean square deviation from ideal values.
f Categories were defined by Molprobity.